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Updated: May 23, 2026
11:01
Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
Retraction: Artificial amidase with modifiable active sites and designable substrate selectivity for aryl amide
1Department of Chemistry, Iowa State University, Ames, Iowa 50011-3111, USA. zhaoy@iastate.edu.
Chemical Communications (Cambridge, England)
|May 22, 2026
Summary
This study reports the retraction of a previously published article concerning artificial amidase enzymes. The original work detailed modifiable active sites and designable substrate selectivity for aryl amide hydrolysis.
Area of Science:
- Biocatalysis and enzyme engineering
- Synthetic chemistry
- Materials science
Background:
- Artificial enzymes offer tunable catalytic properties.
- Designing enzymes with specific substrate selectivity is a key challenge.
- Aryl amide hydrolysis is important in various chemical processes.
Purpose of the Study:
- To report the retraction of a study on artificial amidase.
- To address concerns regarding the findings on enzyme design and selectivity.
- To maintain scientific integrity and accuracy in the field.
Main Methods:
- The retraction notice does not detail specific methods.
- It refers to the original publication for experimental procedures.
- The decision to retract is based on post-publication review.
Main Results:
- The original study claimed the development of artificial amidase with modifiable active sites.
- It reported designable substrate selectivity for aryl amide hydrolysis.
- The retraction indicates issues with the reported results or conclusions.
Conclusions:
- The article 'Artificial amidase with modifiable active sites and designable substrate selectivity for aryl amide hydrolysis' is retracted.
- This retraction is a necessary step to uphold scientific standards.
- Further research in artificial enzyme design should proceed with rigorous validation.
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